What question did this study set out to answer?

Achieve the complete chemical synthesis of a functional transcription factor-related protein complex involving cMyc and Max.

March 1, 1995Journal of the American Chemical Society

Total Chemical Synthesis of a Unique Transcription Factor-Related Protein: cMyc-Max

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Authors

LCLynne E. CanneGryphon Scientific (United States)ADAdrian R. Ferre- D'AmareRockefeller University SBS.K. BurleyRutgers, The State University of New Jersey

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Implication

In vitro chemical synthesis demonstrates the full covalent assembly of transcription factor cMyc-Max, indicating new routes for preparing complex functional regulatory proteins.

Key Points

Achieve the complete chemical synthesis of a functional transcription factor-related protein complex involving cMyc and Max.
Applied total chemical protein synthesis techniques to assemble the polypeptide chains corresponding to transcription factor domains.
Purified synthetic peptide segments and mediated their covalent ligation and folding into native-like macromolecular structures.
Successfully produced the full-length cMyc-Max protein framework through stepwise chemical assembly without biological expression systems.
Demonstrated that chemically synthesized transcription factor domains fold properly and retain the molecular architecture required for specific macromolecular interactions.

Cite This Study

Canne et al. (1995) studied this question.

synapsesocial.com/papers/69d91b2234ded318bb68407c https://doi.org/10.1021/ja00116a005

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Implication

In vitro chemical synthesis demonstrates the full covalent assembly of transcription factor cMyc-Max, indicating new routes for preparing complex functional regulatory proteins.

Total Chemical Synthesis of a Unique Transcription Factor-Related Protein: cMyc-Max

Discussion

Member takes

Implication

Key Points

Cite This Study

Total Chemical Synthesis of a Unique Transcription Factor-Related Protein: cMyc-Max

Discussion

Member takes

Implication

Key Points

Cite This Study

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